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1rds

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[[Image:1rds.gif|left|200px]]<br /><applet load="1rds" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1rds.gif|left|200px]]
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caption="1rds, resolution 1.8&Aring;" />
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'''CRYSTAL STRUCTURE OF RIBONUCLEASE MS (AS RIBONUCLEASE T1 HOMOLOGUE) COMPLEXED WITH A GUANYLYL-3',5'-CYTIDINE ANALOGUE'''<br />
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{{Structure
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|PDB= 1rds |SIZE=350|CAPTION= <scene name='initialview01'>1rds</scene>, resolution 1.8&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=GPC:2'-FLUOROGUANYLYL-(3'-5')-PHOSPHOCYTIDINE'>GPC</scene>
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|ACTIVITY= [http://en.wikipedia.org/wiki/Ribonuclease_T(1) Ribonuclease T(1)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.27.3 3.1.27.3]
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|GENE=
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}}
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'''CRYSTAL STRUCTURE OF RIBONUCLEASE MS (AS RIBONUCLEASE T1 HOMOLOGUE) COMPLEXED WITH A GUANYLYL-3',5'-CYTIDINE ANALOGUE'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1RDS is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Aspergillus_phoenicis Aspergillus phoenicis] with <scene name='pdbligand=GPC:'>GPC</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Ribonuclease_T(1) Ribonuclease T(1)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.27.3 3.1.27.3] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RDS OCA].
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1RDS is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Aspergillus_phoenicis Aspergillus phoenicis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RDS OCA].
==Reference==
==Reference==
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Crystal structure of ribonuclease Ms (as a ribonuclease T1 homologue) complexed with a guanylyl-3',5'-cytidine analogue., Nonaka T, Nakamura KT, Uesugi S, Ikehara M, Irie M, Mitsui Y, Biochemistry. 1993 Nov 9;32(44):11825-37. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=8218254 8218254]
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Crystal structure of ribonuclease Ms (as a ribonuclease T1 homologue) complexed with a guanylyl-3',5'-cytidine analogue., Nonaka T, Nakamura KT, Uesugi S, Ikehara M, Irie M, Mitsui Y, Biochemistry. 1993 Nov 9;32(44):11825-37. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/8218254 8218254]
[[Category: Aspergillus phoenicis]]
[[Category: Aspergillus phoenicis]]
[[Category: Ribonuclease T(1)]]
[[Category: Ribonuclease T(1)]]
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[[Category: hydrolase(endoribonuclease)]]
[[Category: hydrolase(endoribonuclease)]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:49:46 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:50:17 2008''

Revision as of 11:50, 20 March 2008


PDB ID 1rds

Drag the structure with the mouse to rotate
, resolution 1.8Å
Ligands:
Activity: Ribonuclease T(1), with EC number 3.1.27.3
Coordinates: save as pdb, mmCIF, xml



CRYSTAL STRUCTURE OF RIBONUCLEASE MS (AS RIBONUCLEASE T1 HOMOLOGUE) COMPLEXED WITH A GUANYLYL-3',5'-CYTIDINE ANALOGUE


Overview

A ribonuclease T1 homologue, ribonuclease Ms (RNase Ms) from Aspergillus saitoi, has been crystallized as a complex with a substrate analogue GfpC where the 2'-hydroxyl (2'-OH) group of guanosine in guanylyl-3',5'-cytidine (GpC) is replaced by the 2'-fluorine (2'-F) atom to prevent transesterification. The crystal structure of the complex was solved at 1.8-A resolution to a final R-factor of 0.204. The role of His92 (RNase T1 numbering) as the general acid catalyst was confirmed. Of the two alternative candidates for a general base to abstract a proton from the 2'-OH group, His40 and Glu58 were found close to the 2'-F atom, making the decision between the two groups difficult. We then superposed the active site of the RNase Ms/GfpC complex with that of pancreatic ribonuclease S (RNase S) complexed with a substrate analogue UpcA, a phosphonate analogue of uridylyl-3',5'-adenosine (UpA), and found that His12 and His119 of RNase A almost exactly coincided with Glu58 and His92, respectively, of RNase Ms. Similar superposition with a prokaryotic microbial ribonuclease, RNase St [Nakamura, K. T., Iwahashi, K., Yamamoto, Y., Iitaka, Y., Yoshida, N., & Mitsui, Y. (1982) Nature 299, 564-566], also indicated Glu58 as a general base. Thus the present comparative geometrical studies consistently favor, albeit indirectly, the traditional as well as the most recent notion [Steyaert, J., Hallenga, K., Wyns, L., & Stanssens, P. (1990) Biochemistry 29, 9064-9072] that Glu58, rather than His40, must be the general base catalyst in the intact enzymes of the RNase T1 family.

About this Structure

1RDS is a Single protein structure of sequence from Aspergillus phoenicis. Full crystallographic information is available from OCA.

Reference

Crystal structure of ribonuclease Ms (as a ribonuclease T1 homologue) complexed with a guanylyl-3',5'-cytidine analogue., Nonaka T, Nakamura KT, Uesugi S, Ikehara M, Irie M, Mitsui Y, Biochemistry. 1993 Nov 9;32(44):11825-37. PMID:8218254

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